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Database: UniProt
Entry: A0A0M2U5K9_9FIRM
LinkDB: A0A0M2U5K9_9FIRM
Original site: A0A0M2U5K9_9FIRM 
ID   A0A0M2U5K9_9FIRM        Unreviewed;       466 AA.
AC   A0A0M2U5K9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000256|HAMAP-Rule:MF_00423};
DE            EC=2.9.1.1 {ECO:0000256|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteine synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE            Short=Sec synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|HAMAP-Rule:MF_00423};
GN   Name=selA {ECO:0000256|HAMAP-Rule:MF_00423};
GN   ORFNames=SY88_07765 {ECO:0000313|EMBL:KKM11586.1};
OS   Clostridiales bacterium PH28_bin88.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM11586.1, ECO:0000313|Proteomes:UP000034222};
RN   [1] {ECO:0000313|EMBL:KKM11586.1, ECO:0000313|Proteomes:UP000034222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Robbins S., Tyson G.;
RT   "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00423}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-
CC         selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728,
CC         Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533,
CC         ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00423};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000256|PIRSR:PIRSR618319-50};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (bacterial route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00423}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00423}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKM11586.1}.
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DR   EMBL; LAKY01000029; KKM11586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2U5K9; -.
DR   STRING; 1605376.SY88_07765; -.
DR   PATRIC; fig|1605376.3.peg.2528; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000034222; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1150.180; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00423; SelA; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR018319; SelA-like.
DR   InterPro; IPR004534; SelA_trans.
DR   InterPro; IPR025862; SelA_trans_N_dom.
DR   NCBIfam; TIGR00474; selA; 1.
DR   PANTHER; PTHR32328; L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR   PANTHER; PTHR32328:SF0; L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR   Pfam; PF12390; Se-cys_synth_N; 1.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00423};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00423}; Reference proteome {ECO:0000313|Proteomes:UP000034222};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00423}.
FT   DOMAIN          9..48
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   466 AA;  50542 MW;  1418EB34266A4D5D CRC64;
     MDSEQQRLLR SLPAVDEVLQ AEPVKGLLAE APRGLVVEAV REVLEEYRAS IRQDRYPDPV
     TREEVAVSAA KRVRAFLRPH LRRVINATGV VLHTNLGRAV LSRKAREAVQ VAAAGYTNLE
     LDLATGERGS RYHHVNRLLT RLSGAEDALV VNNNAAAVLL ALSTLARGRE VIVSRGQLVE
     IGGSFRVPEV MAQGGAHLVE VGTTNKTYLR DYQAAITPET ALLLKVHTSN YRVVGFTRET
     SLEELVALGR AREIPVMEDL GSGFLVDLTP WGITGEPTVR DSVAKGADVV TFSGDKLLGG
     PQAGIILGRA DLIRKMKAHP LTRALRVDKL TLAALEATLR DYLDLPGARE RIPTLRMLTA
     QVEELQPRAE ELLALLEQQL TGRGALELTA GYSEAGGGSL PTTRIPTMLV TIFPRGVTAD
     ALVARLREQE PAVMARIQDD RVVLDVRTVL PEEIPLLAGA VTACLT
//
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